Crystal structure of human Dipeptidyl Peptidase III. Determined by X-ray diffraction at 1.9 Å resolution. Released 3 Feb 2009.
Explore 3FVY in 3D Show helices and sheets RCSB PDB PDBe
3FVY contains 41 α-helices and 32 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 14-16 | 3 | 1 |
| α-helix | 20-24 | 5 | |
| α-helix | 28-45 | 18 | |
| α-helix | 47-50 | 4 | |
| α-helix | 56-69 | 14 | |
| α-helix | 72-81 | 10 | |
| α-helix | 86-102 | 17 | |
| β-strand | 106 | 1 | 2 |
| β-strand | 112 | 1 | 3 |
| β-strand | 113 | 1 | 2 |
| α-helix | 120-129 | 10 | |
| α-helix | 131-135 | 5 | |
| α-helix | 137-152 | 16 | |
| α-helix | 156-158 | 3 | |
| β-strand | 160 | 1 | 3 |
| β-strand | 161 | 1 | 4 |
| α-helix | 164-166 | 3 | |
| β-strand | 168 | 1 | 4 |
| β-strand | 172 | 1 | 5 |
| α-helix | 178-190 | 13 | |
| β-strand | 198-204 | 7 | 5 |
| β-strand | 210-217 | 8 | 5 |
| α-helix | 231-233 | 3 | |
| β-strand | 236-239 | 4 | 5 |
| β-strand | 242-250 | 9 | 5 |
| α-helix | 252-266 | 15 | |
| α-helix | 272-287 | 16 | |
| α-helix | 290-302 | 13 | |
| β-strand | 308-316 | 9 | 6 |
| α-helix | 326 | 1 | |
| β-strand | 327-334 | 8 | 6 |
| α-helix | 337-348 | 12 | |
| α-helix | 350-355 | 6 | |
| α-helix | 361-363 | 3 | |
| β-strand | 375-376 | 2 | 7 |
| β-strand | 377-382 | 6 | 6 |
| β-strand | 389-392 | 4 | 7 |
| α-helix | 396-401 | 6 | |
| β-strand | 405-409 | 5 | 7 |
| α-helix | 410-413 | 4 | |
| α-helix | 421-423 | 3 | |
| β-strand | 427 | 1 | 8 |
| α-helix | 429-448 | 20 | |
| α-helix | 449-454 | 6 | |
| β-strand | 462 | 1 | 9 |
| β-strand | 463 | 1 | 10 |
| β-strand | 469 | 1 | 10 |
| β-strand | 477 | 1 | 11 |
| β-strand | 484 | 1 | 11 |
| β-strand | 489 | 1 | 9 |
| α-helix | 495-498 | 4 | |
| α-helix | 503-518 | 16 | |
| α-helix | 522-528 | 7 | |
| α-helix | 532-552 | 21 | |
| α-helix | 553-556 | 4 | |
| β-strand | 557-558 | 2 | 12 |
| α-helix | 559-561 | 3 | |
| β-strand | 563-564 | 2 | 12 |
| α-helix | 567-581 | 15 | |
| β-strand | 587-593 | 7 | 8 |
| β-strand | 599-605 | 7 | 8 |
| α-helix | 607-609 | 3 | |
| α-helix | 610-614 | 5 | |
| α-helix | 615-630 | 16 | |
| α-helix | 634-644 | 11 | |
| α-helix | 655-664 | 10 | |
| α-helix | 668-670 | 3 | |
| β-strand | 671-673 | 3 | 1 |
| β-strand | 676-680 | 5 | 13 |
| β-strand | 683-687 | 5 | 13 |
| α-helix | 693-701 | 9 | |
| α-helix | 708-722 | 15 | |
| α-helix | 723-725 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Dipeptidyl-peptidase 3 | A | protein | 728 | Homo sapiens | Q9NY33 (AlphaFold model) |
>3FVY_1 Dipeptidyl-peptidase 3 (chains A) GAMADTQYILPNDIGVSSLDCREAFRLLSPTERLYAYHLSRAAWYGGLAVLLQTSPEAPY IYALLSRLFRAQDPDQLHQHALAEGLTEEEYQAFLVYAAGVYSNMGNYKSFGDTKFVPNL PKEKLERVILGSEAAQQHPEEVRGLWQTCGELMFSLEPRLRHLGLGKEGITTYFSGNCTM EDAKLAQDFLDSQNLSAYNTRLFKEVDGEGKPYYEVRLASVLGSEPSLDSEVTSKLKSYE FRGSPFQVTRGDYAPILQKVVEQLEKAKAYAANSHQGQMLAQYIESFTQGSIEAHKRGSR FWIQDKGPIVESYIGFIESYRDPFGSRGEFEGFVAVVNKAMSAKFERLVASAEQLLKELP WPPTFEKDKFLTPDFTSLDVLTFAGSGIPAGINIPNYDDLRQTEGFKNVSLGNVLAVAYA TQREKLTFLEEDDKDLYILWKGPSFDVQVGLHELLGHGSGKLFVQDEKGAFNFDQETVIN PETGEQIQSWYRSGETWDSKFSTIASSYEECRAESVGLYLCLHPQVLEIFGFEGADAEDV IYVNWLNMVRAGLLALEFYTPEAFNWRQAHMQARFVILRVLLEAGEGLVTITPTTGSDGR PDARVRLDRSKIRSVGKPALERFLRRLQVLKSTGDVAGGRALYEGYATVTDAPPECFLTL RDTVLLRKESRKLIVQPNTRLEGSDVQLLEYEASAAGLIRSFSERFPEDGPELEEILTQL ATADARFW
Water and common crystallization additives (CL) are not listed.
Entropy-driven binding of opioid peptides induces a large domain motion in human dipeptidyl peptidase III. Bezerra, G.A., Dobrovetsky, E., Viertlmayr, R. et al. Proc Natl Acad Sci U S A (2012) 109:6525-6530. DOI 10.1073/pnas.1118005109 · PubMed
Other PDB entries of the same protein (UniProt Q9NY33 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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